Evidence map›Paper›PMID 19923889›Full record

ReviewCell cycle (Georgetown, Tex.)2009

Peroxiredoxin 1 and its role in cell signaling.

Carola A Neumann, Juxiang Cao, Yefim Manevich

Open access · bronzeAbstract readReview
In one paragraph

Review in Cell cycle (Georgetown, Tex.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
123citing papers in PubMed, 1 pooled it
5.5field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

123 citing papers in PubMed, 1 synthesis or guideline pooled it, 261 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Frontiers in microbiology · 2026
    Article
  8. Article
  9. Review
  10. Review
  11. Peroxiredoxin 1 safeguards the nucleolar genome from oxidative damage.bioRxiv : the preprint server for biology · 2025
    Article
  12. Review
  13. Article
  14. Article
  15. A new perspective on iron-dependent cell death: PRDX-1-mediated ferroptosis in tumor cells.Apoptosis : an international journal on programmed cell death · 2025
    Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

63 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Carola A NeumannDepartment of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, Charleston, SC, USA. neumannc@musc.edu
Juxiang Cao
Yefim Manevich
Medical University of South Carolina · US

Funding

The Role of Peroxiredoxin1 & Reactive Oxygen Species in Breast Tumor InitiationR01CA131350 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI NEUMANN, CAROLA ANKE · 2010 to 2014
$1.5M
Role of Prdx 1 in Natural Killer Cells and TumorigenesisK22ES012985 · NIEHS · MEDICAL UNIVERSITY OF SOUTH CAROLINA · PI NEUMANN, CAROLA ANKE · 2005 to 2007
$319k
NCI NIH HHS R01 CA131350NIEHS NIH HHS K22 ES012985
6 · The paper itself

Abstract

Peroxiredoxins (Prdxs) are a family of small (22-27 kDa) nonseleno peroxidases currently known to possess six mammalian isoforms. Although their individual roles in cellular redox regulation and antioxidant protection are quite distinct, they all catalyze peroxide reduction of H(2)O(2), organic hydroperoxides and peroxynitrite. They are found to be expressed ubiquitously and in high levels, suggesting that they are both an ancient and important enzyme family. Prdxs can be divided into three major subclasses: typical 2-cysteine (2-Cys) Prdxs (Prdx1-4), atypical 2-Cys Prdx (Prdx 5) and 1-Cys Prdx (Prdx 6). Recent evidence suggests that 2-Cys peroxiredoxins are more than "just simple peroxidases". This hypothesis has been discussed elegantly in recent review articles, considering "over"-oxidation of the protonated thiolate peroxidatic cysteine and post-translational modification of Prdxs as processes initiating a mechanistic switch from peroxidase to chaperon function. The process of over-oxidation of the peroxidatic cysteine (C(P)) occurs during catalysis in the presence of thioredoxin (Trx), thus rendering the sulfenic moiety to sulfinic acid, which can be reduced by sulfiredoxin (Srx). However, further oxidation to sulfonic acid is believed to promote Prdx degradation or, as recently shown, the formation of oligomeric peroxidase-inactive chaperones with questionable H(2)O(2)-scavenging capacity. In the light of this and given that Prdx1 has recently been shown by us and by others to interact directly with signaling molecules, we will explore the possibility that H(2)O(2) regulates signaling in the cell in a temporal and spatial fashion via oxidizing Prdx1. Therefore, this review will focus on H(2)O(2) modulating cell signaling via Prdxs by discussing: (1) the activity of Prdxs towards H(2)O(2); (2) sub cellular localization and availability of other peroxidases, such as catalase or glutathione peroxidases; (3) the availability of Prdxs reducing systems, such as thioredoxin and sulfiredoxin and lastly, (4) Prdx1 interacting signaling molecules.

Indexed as

AnimalsCatalaseCell CompartmentationGlutathioneHumansHydrogen PeroxideOxidation-ReductionOxidoreductases Acting on Sulfur Group DonorsPeroxidasesPeroxiredoxinsSignal TransductionThioredoxinsCatalaseGlutathioneHydrogen PeroxideOxidoreductases Acting on Sulfur Group DonorsPeroxidasesPeroxiredoxinsSRXN1 protein, humanThioredoxins

Identifiers

PMID19923889
PMCPMC7161701
OpenAlexW2036765113

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.